Abstract
We have used high-resolution triple-axis x-ray diffraction analyses to monitor the defectstructure in tetragonal crystals of hen egg-white lysozyme as a function of x-ray irradiation time.At long irradiation times we observed the expected decrease in peak intensity and increase in theangular extent of the peak breadth. In contrast, the initial stages of irradiation showed relativelycomplex changes in both the peak breadth and the intensity; in fact, during the period from 25 to45 h of irradiation the angular breadth of the intensity (both the full-width at half-maximum andthe full-width at 1% of the maximum intensity) decreased to a minimum value. We have foundthat the unambiguous analysis of defects at high angular resolution is complicated by the fact thatthe diffraction characteristics of protein crystals apparently lie at the confluence of the kinematic(ideally imperfect) and dynamic (ideally perfect) treatments of diffraction.
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